TM9S3_HUMAN - dbPTM
TM9S3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TM9S3_HUMAN
UniProt AC Q9HD45
Protein Name Transmembrane 9 superfamily member 3
Gene Name TM9SF3
Organism Homo sapiens (Human).
Sequence Length 589
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MRPLPGALGVAAAAALWLLLLLLPRTRADEHEHTYQDKEEVVLWMNTVGPYHNRQETYKYFSLPFCVGSKKSISHYHETLGEALQGVELEFSGLDIKFKDDVMPATYCEIDLDKEKRDAFVYAIKNHYWYQMYIDDLPIWGIVGEADENGEDYYLWTYKKLEIGFNGNRIVDVNLTSEGKVKLVPNTKIQMSYSVKWKKSDVKFEDRFDKYLDPSFFQHRIHWFSIFNSFMMVIFLVGLVSMILMRTLRKDYARYSKEEEMDDMDRDLGDEYGWKQVHGDVFRPSSHPLIFSSLIGSGCQIFAVSLIVIIVAMIEDLYTERGSMLSTAIFVYAATSPVNGYFGGSLYARQGGRRWIKQMFIGAFLIPAMVCGTAFFINFIAIYYHASRAIPFGTMVAVCCICFFVILPLNLVGTILGRNLSGQPNFPCRVNAVPRPIPEKKWFMEPAVIVCLGGILPFGSIFIEMYFIFTSFWAYKIYYVYGFMMLVLVILCIVTVCVTIVCTYFLLNAEDYRWQWTSFLSAASTAIYVYMYSFYYYFFKTKMYGLFQTSFYFGYMAVFSTALGIMCGAIGYMGTSAFVRKIYTNVKID
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
47PhosphorylationEVVLWMNTVGPYHNR
HEEEEEECCCCCCCC		15.6723663014
51PhosphorylationWMNTVGPYHNRQETY
EEECCCCCCCCHHHC		13.0523663014
57PhosphorylationPYHNRQETYKYFSLP
CCCCCHHHCEEEECC		19.5823663014
59UbiquitinationHNRQETYKYFSLPFC
CCCHHHCEEEECCEE		47.4421890473
59UbiquitinationHNRQETYKYFSLPFC
CCCHHHCEEEECCEE		47.4421890473
70AcetylationLPFCVGSKKSISHYH
CCEECCCCCCHHHHH		44.6126051181
71UbiquitinationPFCVGSKKSISHYHE
CEECCCCCCHHHHHH		55.51-
1162-HydroxyisobutyrylationEIDLDKEKRDAFVYA
EEECCHHHHHHHEEE		62.41-
122PhosphorylationEKRDAFVYAIKNHYW
HHHHHHEEEECCCEE		8.99-
128PhosphorylationVYAIKNHYWYQMYID
EEEECCCEEEEEEEC		18.4023401153
130PhosphorylationAIKNHYWYQMYIDDL
EECCCEEEEEEECCC		4.0023401153
133PhosphorylationNHYWYQMYIDDLPIW
CCEEEEEEECCCCEE		5.9123401153
153PhosphorylationADENGEDYYLWTYKK
CCCCCCEEEEEEEEE		8.9923401153
154PhosphorylationDENGEDYYLWTYKKL
CCCCCEEEEEEEEEE		14.2123401153
157PhosphorylationGEDYYLWTYKKLEIG
CCEEEEEEEEEEEEC		23.9123401153
160UbiquitinationYYLWTYKKLEIGFNG
EEEEEEEEEEECCCC		40.72-
174N-linked_GlycosylationGNRIVDVNLTSEGKV
CCEEEEEEECCCCEE		32.8917660510
174N-linked_GlycosylationGNRIVDVNLTSEGKV
CCEEEEEEECCCCEE		32.8919349973
182UbiquitinationLTSEGKVKLVPNTKI
ECCCCEEEECCCCEE		47.45-
196AcetylationIQMSYSVKWKKSDVK
EEEEEEEEEECCCCC		47.5624885463
198AcetylationMSYSVKWKKSDVKFE
EEEEEEEECCCCCHH		36.3628641951
203UbiquitinationKWKKSDVKFEDRFDK
EEECCCCCHHHHHHH		48.29-
210UbiquitinationKFEDRFDKYLDPSFF
CHHHHHHHHCCHHHH		45.0321890473
2102-HydroxyisobutyrylationKFEDRFDKYLDPSFF
CHHHHHHHHCCHHHH		45.03-
210UbiquitinationKFEDRFDKYLDPSFF
CHHHHHHHHCCHHHH		45.0321890473
252PhosphorylationMRTLRKDYARYSKEE
HHHHHHHHHHHCCHH		8.9426074081
255PhosphorylationLRKDYARYSKEEEMD
HHHHHHHHCCHHHHC		18.8726074081
256PhosphorylationRKDYARYSKEEEMDD
HHHHHHHCCHHHHCC		28.2126074081
257UbiquitinationKDYARYSKEEEMDDM
HHHHHHCCHHHHCCC		61.2821890473
266MethylationEEMDDMDRDLGDEYG
HHHCCCCCCCHHHCC		34.12115917229
272PhosphorylationDRDLGDEYGWKQVHG
CCCCHHHCCCCCCCC		32.7826074081
419N-linked_GlycosylationVGTILGRNLSGQPNF
HHHHHCCCCCCCCCC		36.44UniProtKB CARBOHYD
441UbiquitinationPRPIPEKKWFMEPAV
CCCCCCCCCCCCCHH		43.96-
544PhosphorylationYFFKTKMYGLFQTSF
HHHHHHHHCCCCHHH		16.5423401153
549PhosphorylationKMYGLFQTSFYFGYM
HHHCCCCHHHHHHHH		17.3023401153
550PhosphorylationMYGLFQTSFYFGYMA
HHCCCCHHHHHHHHH		13.7323401153
552PhosphorylationGLFQTSFYFGYMAVF
CCCCHHHHHHHHHHH		8.8923401153
555PhosphorylationQTSFYFGYMAVFSTA
CHHHHHHHHHHHHHH		3.3623401153
560PhosphorylationFGYMAVFSTALGIMC
HHHHHHHHHHHHHHH		13.2323403867
575PhosphorylationGAIGYMGTSAFVRKI
HHHHHHCHHHHHHHH		10.6023401153
576PhosphorylationAIGYMGTSAFVRKIY
HHHHHCHHHHHHHHH		17.6123403867
587UbiquitinationRKIYTNVKID-----
HHHHHCCCCC-----		43.1321890473
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TM9S3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TM9S3_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TM9S3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STOM_HUMANSTOMphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TM9S3_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174, AND MASSSPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-174, AND MASSSPECTROMETRY.

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